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Database: UniProt
Entry: I4ES91_9ACTN
LinkDB: I4ES91_9ACTN
Original site: I4ES91_9ACTN 
ID   I4ES91_9ACTN            Unreviewed;       461 AA.
AC   I4ES91;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=Rhodanese-related sulfurtransferase {ECO:0000313|EMBL:CCH86254.1};
GN   OrderedLocusNames=MODMU_0802 {ECO:0000313|EMBL:CCH86254.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86254.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH86254.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH86254.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
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DR   EMBL; FO203431; CCH86254.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4ES91; -.
DR   STRING; 477641.MODMU_0802; -.
DR   KEGG; mmar:MODMU_0802; -.
DR   PATRIC; fig|477641.3.peg.750; -.
DR   eggNOG; COG0491; Bacteria.
DR   eggNOG; COG0607; Bacteria.
DR   HOGENOM; CLU_030571_7_1_11; -.
DR   OMA; QGAYYIT; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   CDD; cd00158; RHOD; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044528; POD-like_MBL-fold.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR   PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT   DOMAIN          365..451
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   461 AA;  49850 MW;  E8C0231C7A586840 CRC64;
     MIQIETIETS SLGDRSYLAS DGEIAVVVDP QRDIDRVLDL VDKRGVRVTH VLETHIHNDY
     VTGGLELAQR TGAAYVVPAD SGAEFDHLPA GDGEEFQAGR MRLRALHTPG HTHHHMSYAL
     ENADGDVEAV FTGGSMLYGS TGRTDLVSPE DTVGLTHAQY HSVQRLAREL PAETGVFPTH
     GFGSFCSATP TSGTASTVGE QRRVNPALTS AEQDYVDTLL AGLDAFPAYY AHMGPINRQG
     PRPVDLSLPQ LVDPAELRRR IEAGEWVVDL RERTAFAAGH LTDSLNFELG DNFVTYLGWL
     YRWGAPLTLI GESEEQVAEA RRQLVRIGID ELAGAAVGNI ETLAHGAQLR SYEVSDFASL
     AEAVRQGPVQ VLDARRDDER AQGGVRDSQH IPLHELNDRI GEVPEGEVWV YCGSGYRASI
     AASVLDRPGR QVVLINDSYG AAAEAGLEDE RPTEGAGSPT A
//
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